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Protein

Peroxisome biogenesis factor 1

Gene

Pex1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for stability of PEX5 and protein import into the peroxisome matrix. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi600 – 6078ATPSequence Analysis
Nucleotide bindingi882 – 8898ATPSequence Analysis

GO - Molecular functioni

  1. ATPase activity, coupled Source: MGI
  2. ATP binding Source: MGI
  3. lipid binding Source: UniProtKB-KW
  4. protein complex binding Source: MGI
  5. protein C-terminus binding Source: MGI

GO - Biological processi

  1. ATP catabolic process Source: MGI
  2. microtubule-based peroxisome localization Source: MGI
  3. peroxisome organization Source: MGI
  4. protein import into peroxisome matrix Source: MGI
  5. protein targeting to peroxisome Source: MGI
Complete GO annotation...

Keywords - Biological processi

Peroxisome biogenesis, Protein transport, Transport

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisome biogenesis factor 1
Alternative name(s):
Peroxin-1
Gene namesi
Name:Pex1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1918632. Pex1.

Subcellular locationi

Cytoplasm By similarity. Peroxisome membrane By similarity
Note: Associated with peroxisomal membranes.By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. intracellular membrane-bounded organelle Source: MGI
  5. peroxisomal membrane Source: MGI
  6. peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi135 – 1351R → A: Loss of phospholipid-binding. 1 Publication
Mutagenesisi174 – 1741K → A: No effect on phospholipid-binding. 1 Publication

Keywords - Diseasei

Peroxisome biogenesis disorder

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12841284Peroxisome biogenesis factor 1PRO_0000304931Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki834 – 834Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei1210 – 12101PhosphoserineBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ5BL07.
PaxDbiQ5BL07.
PRIDEiQ5BL07.

PTM databases

PhosphoSiteiQ5BL07.

Expressioni

Gene expression databases

BgeeiQ5BL07.
CleanExiMM_PEX1.
ExpressionAtlasiQ5BL07. baseline and differential.
GenevestigatoriQ5BL07.

Interactioni

Subunit structurei

Interacts directly with PEX6. Interacts indirectly with PEX26, via its interaction with PEX6 (By similarity).By similarity

Protein-protein interaction databases

BioGridi214674. 1 interaction.

Structurei

Secondary structure

1
1284
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 228Combined sources
Beta strandi25 – 273Combined sources
Beta strandi29 – 313Combined sources
Helixi33 – 386Combined sources
Beta strandi47 – 537Combined sources
Beta strandi56 – 583Combined sources
Beta strandi60 – 623Combined sources
Beta strandi73 – 775Combined sources
Helixi78 – 836Combined sources
Beta strandi91 – 966Combined sources
Beta strandi104 – 1129Combined sources
Helixi113 – 1219Combined sources
Helixi126 – 1338Combined sources
Beta strandi142 – 1509Combined sources
Beta strandi152 – 16211Combined sources
Beta strandi165 – 1684Combined sources
Beta strandi174 – 1774Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLFX-ray2.05A3-181[»]
ProteinModelPortaliQ5BL07.
SMRiQ5BL07. Positions 13-179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5BL07.

Family & Domainsi

Domaini

The N-terminal domain shows evolutionary conservation with that of VCP, and is able to bind phospholipids with a preference for phosphatidylinositol monophosphates.

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00550000075032.
HOGENOMiHOG000252959.
HOVERGENiHBG008169.
InParanoidiQ5BL07.
KOiK13338.
OMAiVHSWEKE.
OrthoDBiEOG7W9RT0.
PhylomeDBiQ5BL07.
TreeFamiTF106447.

Family and domain databases

Gene3Di3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR029067. CDC48_domain_2-like.
IPR027417. P-loop_NTPase.
IPR015343. Peroxisome_synth_fac_1_a/b.
IPR015342. PEX-1N.
IPR025653. Pex1.
[Graphical view]
PANTHERiPTHR23077:SF12. PTHR23077:SF12. 1 hit.
PfamiPF00004. AAA. 2 hits.
PF09262. PEX-1N. 1 hit.
PF09263. PEX-2N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5BL07-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MWSSDRLAGA GSGGAVVTVA FTNARDCFLH LPRRLVAQLH LLQNQAIEVA
60 70 80 90 100
SDHQPTYLSW VEGRHFNDQS ENVAEINRQV GQKLGLSSGD QVFLRPCSHV
110 120 130 140 150
VSCQQVEVEP LSADDWEILE LHAISLEQHL LDQIRIVFPK AVVPIWVDQQ
160 170 180 190 200
TYIFIQIVTL MPAAPYGRLE TNTKLLIQPK TRQAKESTFP KEGDAHGQVH
210 220 230 240 250
SYGREQKGLS KELQTRQLHT NSEGITASNG RDPKVPGGPL KPSWWAVLGS
260 270 280 290 300
MLSFGPDSKQ ESAWGSLELG AFKNMQSQAA PLEGTFRVCQ VQPPSARTTT
310 320 330 340 350
ATSVFHKHCT AHVFPWDQEY FDVEPSFTVT YGKLVKLHSP KQQQDKSKQG
360 370 380 390 400
VLLPDKEKQL SKSPDHKQIS SNRSEEAAEA CVLKVVWNGL EELKNATEFT
410 420 430 440 450
ESLELLHRGK VWIPDDLRKR LNIEMHAVVR ITPLETTPKI PRSLKLQPRE
460 470 480 490 500
NLPKDVNEET IKTVFSSWVQ QSATTMLPLV ISKEERIKLE IKDGLREFSL
510 520 530 540 550
STVHSQEKEK EEGKTVFVLS SILLQKISVQ VLLEPMIKEE QSAEIDFLLP
560 570 580 590 600
SLTLSSLGGV SALGASAMEH ITHSLLGRPL SRQLMALVAG LRNGALLITG
610 620 630 640 650
GKGSGKSTFA KAICKEAQDT LDARVETVDC KALRGKRLES IQKALEVAFS
660 670 680 690 700
EAAWRQPSVI LLDDLDLIAG LPSVPEQEHS PEAVQSQRLA HALNDMIKEF
710 720 730 740 750
VSTGSLVALI ATSQLQQSLH PSLVSAQGIH TFQCVQHLQP PNPEQRCEIL
760 770 780 790 800
HSVVKNKLGC DISNFPDLDL QCIAKDTEAF VARDFTVLVD RAIHSSLSRQ
810 820 830 840 850
HSSSREDLTL TTSDFQKALR GFLPASLRNV NLHKPRDLGW DKIGGLHEVR
860 870 880 890 900
QILMDTIQLP AKYPELFANL PIRQRTGILL YGPPGTGKTL LAGVVARESG
910 920 930 940 950
MNFISIKGPE LLSKYIGASE QAVRDVFIRA QAAKPCILFF DEFESIAPRR
960 970 980 990 1000
GHDNTGVTDR VVNQLLTQLD GVEGLQGVYV LAATSRPDLI DPALLRPGRL
1010 1020 1030 1040 1050
DKCVYCPPPD QVSRLEILTV LSKSLALADD VDLQHVASVT DSFTGADLKA
1060 1070 1080 1090 1100
LLYNAQLEAL QGRLLPSGLP DGGSSSDSDL SLSSMVFLNH SSGSDDSAGD
1110 1120 1130 1140 1150
GECGLEQSLL SLEMSEILPD ESKFNMYRLY FGSSYESELG NGTPSDLSSH
1160 1170 1180 1190 1200
CLSAPSSVTQ DLPAAPGKDP LFTQHPVFRT PSQEGCQDLT QEQRDQLRAE
1210 1220 1230 1240 1250
ISIIKGRYRS QSGEDESLNQ PGPIKTTFAI SQAHLMTALA HTRPSISEDE
1260 1270 1280
GKEFAELYEN FQNPKKRKNQ SGTVFRTGQK VTLA
Length:1,284
Mass (Da):141,428
Last modified:October 2, 2007 - v2
Checksum:i29B6C9B6E93FA6EF
GO
Isoform 2 (identifier: Q5BL07-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     413-452: Missing.

Note: No experimental confirmation available.

Show »
Length:1,244
Mass (Da):136,743
Checksum:i9B1073BBA4CC4106
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei413 – 45240Missing in isoform 2. 1 PublicationVSP_028131Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC090845 mRNA. Translation: AAH90845.1.
AK017309 mRNA. Translation: BAB30684.1.
AK149599 mRNA. Translation: BAE28984.1.
CCDSiCCDS19065.1. [Q5BL07-2]
RefSeqiNP_001280735.1. NM_001293806.1. [Q5BL07-1]
NP_082053.1. NM_027777.2. [Q5BL07-2]
UniGeneiMm.379196.

Genome annotation databases

EnsembliENSMUST00000006061; ENSMUSP00000006061; ENSMUSG00000005907. [Q5BL07-2]
ENSMUST00000121291; ENSMUSP00000113304; ENSMUSG00000005907. [Q5BL07-1]
GeneIDi71382.
KEGGimmu:71382.
UCSCiuc008whf.1. mouse. [Q5BL07-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC090845 mRNA. Translation: AAH90845.1.
AK017309 mRNA. Translation: BAB30684.1.
AK149599 mRNA. Translation: BAE28984.1.
CCDSiCCDS19065.1. [Q5BL07-2]
RefSeqiNP_001280735.1. NM_001293806.1. [Q5BL07-1]
NP_082053.1. NM_027777.2. [Q5BL07-2]
UniGeneiMm.379196.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLFX-ray2.05A3-181[»]
ProteinModelPortaliQ5BL07.
SMRiQ5BL07. Positions 13-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214674. 1 interaction.

PTM databases

PhosphoSiteiQ5BL07.

Proteomic databases

MaxQBiQ5BL07.
PaxDbiQ5BL07.
PRIDEiQ5BL07.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006061; ENSMUSP00000006061; ENSMUSG00000005907. [Q5BL07-2]
ENSMUST00000121291; ENSMUSP00000113304; ENSMUSG00000005907. [Q5BL07-1]
GeneIDi71382.
KEGGimmu:71382.
UCSCiuc008whf.1. mouse. [Q5BL07-2]

Organism-specific databases

CTDi5189.
MGIiMGI:1918632. Pex1.

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00550000075032.
HOGENOMiHOG000252959.
HOVERGENiHBG008169.
InParanoidiQ5BL07.
KOiK13338.
OMAiVHSWEKE.
OrthoDBiEOG7W9RT0.
PhylomeDBiQ5BL07.
TreeFamiTF106447.

Miscellaneous databases

EvolutionaryTraceiQ5BL07.
NextBioi333669.
PROiQ5BL07.
SOURCEiSearch...

Gene expression databases

BgeeiQ5BL07.
CleanExiMM_PEX1.
ExpressionAtlasiQ5BL07. baseline and differential.
GenevestigatoriQ5BL07.

Family and domain databases

Gene3Di3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR029067. CDC48_domain_2-like.
IPR027417. P-loop_NTPase.
IPR015343. Peroxisome_synth_fac_1_a/b.
IPR015342. PEX-1N.
IPR025653. Pex1.
[Graphical view]
PANTHERiPTHR23077:SF12. PTHR23077:SF12. 1 hit.
PfamiPF00004. AAA. 2 hits.
PF09262. PEX-1N. 1 hit.
PF09263. PEX-2N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-505 AND 795-1284 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Head and Liver.
  3. "The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97."
    Shiozawa K., Goda N., Shimizu T., Mizuguchi K., Kondo N., Shimozawa N., Shirakawa M., Hiroaki H.
    FEBS J. 273:4959-4971(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHOLIPID BINDING, MUTAGENESIS OF ARG-135 AND LYS-174.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain."
    Shiozawa K., Maita N., Tomii K., Seto A., Goda N., Akiyama Y., Shimizu T., Shirakawa M., Hiroaki H.
    J. Biol. Chem. 279:50060-50068(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 3-181.

Entry informationi

Entry nameiPEX1_MOUSE
AccessioniPrimary (citable) accession number: Q5BL07
Secondary accession number(s): Q3UEC7, Q9CU85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: March 4, 2015
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.